Research workbench
Cocrystal structure of the flagellar SIGMA/ANTI-sigma complex, sigma- 28/FLGM
Analyse Cocrystal structure of the flagellar SIGMA/ANTI-sigma complex, sigma- 28/FLGM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RP3
- Type
- protein
- Length
- 1,211 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase sigma factor sigma-28 (flia); Anti sigma factor flgm
- UniProt
- O67268
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 8 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase sigma factor sigma-28 (flia) | protein | 235 | 78% helix, 0% strand | O67268 |
| B | Anti sigma factor flgm | protein | 77 | 66% helix, 0% strand | O67268 |
| C | RNA polymerase sigma factor sigma-28 (flia) | protein | 234 | 79% helix, 0% strand | O67268 |
| D | Anti sigma factor flgm | protein | 70 | 80% helix, 0% strand | O67268 |
| E | RNA polymerase sigma factor sigma-28 (flia) | protein | 235 | 78% helix, 0% strand | O67268 |
| F | Anti sigma factor flgm | protein | 64 | 73% helix, 0% strand | O67268 |
| G | RNA polymerase sigma factor sigma-28 (flia) | protein | 226 | 79% helix, 0% strand | O67268 |
| H | Anti sigma factor flgm | protein | 70 | 71% helix, 0% strand | O67268 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 795 | 0.81 | 0.84 | 84 | empty |
| 2 | 522 | 0.76 | 0.84 | 55 | empty |
| 3 | 364 | 0.69 | 0.82 | 46 | empty |
| 4 | 300 | 0.61 | 0.79 | 39 | empty |
| 5 | 137 | 0.61 | 0.85 | 24 | empty |
Interfaces
11 interfaces between chains.
- G–H · 2065 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 2016 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 2013 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1920 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 546 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1RP3 · Cocrystal structure of the flagellar sigma/anti-sigma complex, Sigma-28/FlgM · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O67268
- Elsewhere: RCSB PDB 1RP3 · PDBe 1RP3 · UniProt O67268
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